Quantitative Analysis of Glycated Proteins

Priego-Capote, Feliciano; Ramírez-Boo, M.; Finamore, Francesco; Gluck, Florent; Sanchez, Jean‐Charles

doi:10.1021/pr4000398

Cited by 21 publications

(13 citation statements)

References 31 publications

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“…Notably, at pH 4 the enzyme cleaves preferentially at the C terminus of Glu whereas at pH 8 it additionally accepts Asp. Due to the fact that Glu and Asp are not modified by glycation, Glu‐C is proposed in methodologies for large‐scale qualitative and quantitative analysis of glycated proteins in complex biological samples such as plasma or red blood cells . Besides multi‐protease studies aiming at improved proteome coverage, Glu‐C has also often been used for the study of highly modified proteins like histones using middle‐down proteomics approaches .…”

Section: Runner‐up Proteases In Proteomicsmentioning

confidence: 99%

Proteomics beyond trypsin

Tsiatsiani¹,

Heck²

2015

The FEBS Journal

284

329

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Peptide-centered shotgun analysis of proteins has been the core technology in mass spectrometry based proteomics and has enabled numerous biological discoveries, such as the large-scale charting of protein-protein interaction networks, the quantitative analysis of protein post-translational modifications and even the first drafts of the human proteome. The conversion of proteins into peptides in these so-called bottom-up approaches is nearly uniquely done by using trypsin as a proteolytic reagent. Here, we argue that our view of the proteome still remains incomplete and this is partially due to the nearly exclusive use of trypsin. Newly emerging alternative proteases and/or multi-protease protein digestion aim to increase proteome sequence coverage and improve the identification of post-translational modifications, through the analysis of complementary and often longer peptides, introducing an approach termed middle-down proteomics. Of pivotal importance for this purpose is the identification of proteases beneficial for use in proteomics. Here, we describe some of the shortcomings of the nearly exclusive use of trypsin in proteomics and review the properties of other proteomics-appropriate proteases. We describe favorable protease traits with an emphasis on middle-down proteomics and suggest potential sources for the discovery of new proteases. We also highlight a few examples wherein the use of other proteases than trypsin enabled the generation of more comprehensive data sets leading to previously unexplored knowledge of the proteome.

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Section: Runner‐up Proteases In Proteomicsmentioning

confidence: 99%

Proteomics beyond trypsin

Tsiatsiani¹,

Heck²

2015

The FEBS Journal

284

329

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show abstract

“…In contrast to TDP approach, the bottom-up proteomic (BUP) strategy can be applied to protein mixtures of any composition and complexity [ 114 ]. It relies on: (i) separation of proteins; (ii) limited proteolysis; (iii) separation of resulted cleavage peptides; (iv) their identification by tandem mass spectrometry (MS/MS); and (v) annotation of individual protein sequence tags [ 123 , 131 , 132 , 133 ]. In application to sugar-modified proteins, BUP provides detailed information about glycoprotein profile and gives an access to specific mapping of glycosylation sites [ 134 ].…”

Section: Part 1 Probing the Structure Of Glycated Proteins By Masmentioning

confidence: 99%

“…Thus, 18 O-labeling of HSA peptides was successfully applied for characterization of glycation dynamics [ 59 , 248 ] and early diagnostics of T2DM [ 249 ]. Another informative labeling technique relies on incubation with [ 13 C 6 ]glucose under the conditions mimicking in vivo glycation [ 131 , 151 , 221 ]. In terms of this approach, relative quantification relied on doublet signals representing in vivo glycation with [ 12 C 6 ]glucose and in vitro incorporation of [ 13 C 6 ]glucose [ 131 , 151 , 250 ].…”

Section: Part 1 Probing the Structure Of Glycated Proteins By Masmentioning

confidence: 99%

“…Another informative labeling technique relies on incubation with [ 13 C 6 ]glucose under the conditions mimicking in vivo glycation [ 131 , 151 , 221 ]. In terms of this approach, relative quantification relied on doublet signals representing in vivo glycation with [ 12 C 6 ]glucose and in vitro incorporation of [ 13 C 6 ]glucose [ 131 , 151 , 250 ]. Finally, standard isotope dilution techniques might rely on synthetic 13 C, 15 N-labeled peptides, spiked to plasma samples for a high-throughput characterization of their glycated profiles by multiple reaction monitoring [ 189 ].…”

Section: Part 1 Probing the Structure Of Glycated Proteins By Masmentioning

confidence: 99%

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Maillard Proteomics: Opening New Pages

Soboleva

Schmidt

Vikhnina

et al. 2017

IJMS

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Protein glycation is a ubiquitous non-enzymatic post-translational modification, formed by reaction of protein amino and guanidino groups with carbonyl compounds, presumably reducing sugars and α-dicarbonyls. Resulting advanced glycation end products (AGEs) represent a highly heterogeneous group of compounds, deleterious in mammals due to their pro-inflammatory effect, and impact in pathogenesis of diabetes mellitus, Alzheimer’s disease and ageing. The body of information on the mechanisms and pathways of AGE formation, acquired during the last decades, clearly indicates a certain site-specificity of glycation. It makes characterization of individual glycation sites a critical pre-requisite for understanding in vivo mechanisms of AGE formation and developing adequate nutritional and therapeutic approaches to reduce it in humans. In this context, proteomics is the methodology of choice to address site-specific molecular changes related to protein glycation. Therefore, here we summarize the methods of Maillard proteomics, specifically focusing on the techniques providing comprehensive structural and quantitative characterization of glycated proteome. Further, we address the novel break-through areas, recently established in the field of Maillard research, i.e., in vitro models based on synthetic peptides, site-based diagnostics of metabolism-related diseases (e.g., diabetes mellitus), proteomics of anti-glycative defense, and dynamics of plant glycated proteome during ageing and response to environmental stress.

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“…Reconstituted peptides were fractionated by boronate affinity chromatography by the interaction between the hydroxylgroups of glycated peptides, present at low concentrations, and boronic acid, as previously described [28,29]. For this purpose, samples (50 L) were injected in a Waters 600E HPLC system equipped with a TSK-Gel boronate affinity column from Tosoh Bioscience (7.5 cm length × 7.5 mm inner diameter, i.d., 10 m particle size).…”

Section: Enrichment Of Glycated Peptides Using Boronate Affinity Chromentioning

confidence: 99%

Aspirin-mediated acetylation of haemoglobin increases in presence of high glucose concentration and decreases protein glycation

Finamore

Priego-Capote

Nolli³

et al. 2015

EuPA Open Proteomics

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Aspirin-mediated acetylationRed blood cells Haemoglobin Mass spectrometry Label-free a b s t r a c t Glycation represents the first stage in the development of diabetic complications. Aspirin was shown to prevent sugars reacting with proteins, but the exact mechanism of this interaction was not well defined. We performed a quantitative analysis to calculate the levels of acetylation and glycation of haemoglobin, among others red blood cell (RBC) proteins, using a label free approach. After glucose incubation, increases in the acetylation levels were seen for several haemoglobin subunits, while a parallel decrease of their glycation levels was observed after aspirin incubation. These results suggest that, a mutual influence between these two modifications, occur at protein level.

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Quantitative Analysis of Glycated Proteins

Cited by 21 publications

References 31 publications

Proteomics beyond trypsin

Proteomics beyond trypsin

Maillard Proteomics: Opening New Pages

Aspirin-mediated acetylation of haemoglobin increases in presence of high glucose concentration and decreases protein glycation

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